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Conserved domains on  [gi|446749021|ref|WP_000826277|]
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MULTISPECIES: propanediol utilization protein PduV [Enterobacteriaceae]

Protein Classification

EutP/PduV family microcompartment system protein( domain architecture ID 10566397)

EutP/PduV family microcompartment system protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PduV-EutP pfam10662
Ethanolamine utilization - propanediol utilization; Members of this family function in ...
 1-136 1.99e-85

Ethanolamine utilization - propanediol utilization; Members of this family function in ethanolamine and propanediol degradation pathways. PduV may be involved in the association of the bacterial microcompartments (BMCs) to filaments.


:

Pssm-ID: 402341 [Multi-domain]  Cd Length: 137  Bit Score: 246.04  E-value: 1.99e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446749021    1 MKRLMFIGPSQCGKTSLTQSLRGEALHYKKTQAIEWSPMAIDTPGEYLENRCLYSALLTSACEADVIALVLNADAQWSPF 80
Cdd:pfam10662   1 MKKIMLIGPTGCGKTTLCQALSGEELKYKKTQAIEFYDNAIDTPGEYLENRRYYSALIVTSADADVIALVQDATEPESTF 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 446749021   81 SPGFTAPMNRPTIGLVTKADLAE-PQRISLVAEWLTQAGAQQIFITSALNNSGLDAV 136
Cdd:pfam10662  81 PPGFASMFNKPVIGIITKIDLAKdEANIEIAEEWLSLAGAQKIFRISAVEKIGIEEL 137
 
Name Accession Description Interval E-value
PduV-EutP pfam10662
Ethanolamine utilization - propanediol utilization; Members of this family function in ...
 1-136 1.99e-85

Ethanolamine utilization - propanediol utilization; Members of this family function in ethanolamine and propanediol degradation pathways. PduV may be involved in the association of the bacterial microcompartments (BMCs) to filaments.


Pssm-ID: 402341 [Multi-domain]  Cd Length: 137  Bit Score: 246.04  E-value: 1.99e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446749021    1 MKRLMFIGPSQCGKTSLTQSLRGEALHYKKTQAIEWSPMAIDTPGEYLENRCLYSALLTSACEADVIALVLNADAQWSPF 80
Cdd:pfam10662   1 MKKIMLIGPTGCGKTTLCQALSGEELKYKKTQAIEFYDNAIDTPGEYLENRRYYSALIVTSADADVIALVQDATEPESTF 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 446749021   81 SPGFTAPMNRPTIGLVTKADLAE-PQRISLVAEWLTQAGAQQIFITSALNNSGLDAV 136
Cdd:pfam10662  81 PPGFASMFNKPVIGIITKIDLAKdEANIEIAEEWLSLAGAQKIFRISAVEKIGIEEL 137
EutP TIGR02528
ethanolamine utilization protein, EutP; This protein is found within operons which code for ...
 2-142 7.51e-83

ethanolamine utilization protein, EutP; This protein is found within operons which code for polyhedral organelles containing the enzyme ethanolamine ammonia lyase. The function of this gene is unknown, although the presence of an N-terminal GxxGxGK motif implies a GTP-binding site. [Energy metabolism, Amino acids and amines]


Pssm-ID: 131580 [Multi-domain]  Cd Length: 142  Bit Score: 239.65  E-value: 7.51e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446749021    2 KRLMFIGPSQCGKTSLTQSLRGEALHYKKTQAIEWSPMAIDTPGEYLENRCLYSALLTSACEADVIALVLNADAQWSPFS 81
Cdd:TIGR02528   1 KRIMFIGSVGCGKTTLTQALQGEEILYKKTQAVEYNDGAIDTPGEYVENRRLYSALIVTAADADVIALVQSATDPESRFP 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446749021   82 PGFTAPMNRPTIGLVTKADLAE-PQRISLVAEWLTQAGAQQIFITSALNNSGLDAVLDFLNS 142
Cdd:TIGR02528  81 PGFASIFVKPVIGLVTKIDLAEaDVDIERAKELLETAGAEPIFEISSVDEQGLEALVDYLNS 142
EutP COG4917
Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport ...
 1-144 2.12e-77

Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport and metabolism];


Pssm-ID: 443945 [Multi-domain]  Cd Length: 145  Bit Score: 226.22  E-value: 2.12e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446749021   1 MKRLMFIGPSQCGKTSLTQSLRGEALHYKKTQAIEWSPMAIDTPGEYLENRCLYSALLTSACEADVIALVLNADAQWSPF 80
Cdd:COG4917    1 MKRIMLIGRSGAGKTTLTQALNGEELEYRKTQAVEYYDNIIDTPGEYIENPRFYKALIATAQDADVIVLVQDATEPRSVF 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446749021  81 SPGFTAPMNRPTIGLVTKADLAEPQrISLVAEWLTQAGAQQIFITSALNNSGLDAVLDFLNSKE 144
Cdd:COG4917   81 PPGFAKAFNKPVIGVITKIDLPEAD-VERARKWLKSAGVEPIFIVSSVTGEGIEELKEYLEELG 143
PRK15467 PRK15467
ethanolamine utilization acetate kinase EutP;
1-142 1.32e-13

ethanolamine utilization acetate kinase EutP;


Pssm-ID: 185364 [Multi-domain]  Cd Length: 158  Bit Score: 64.22  E-value: 1.32e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446749021   1 MKRLMFIGPSQCGKTSLTQSLRGEALHYKKTQAIEWSPMA-IDTPGEYLENRCLYSALLTSACEADVIALVLNADAQWSP 79
Cdd:PRK15467   1 MKRIAFVGAVGAGKTTLFNALQGNYTLARKTQAVEFNDKGdIDTPGEYFSHPRWYHALITTLQDVDMLIYVHGANDPESR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446749021  80 FSPG-FTAPMNRPTIGLVTKADLAEPQrISLVAEWLTQAGAQQ-IFITSALNNSGLDAVLDFLNS 142
Cdd:PRK15467  81 LPAGlLDIGVSKRQIAVISKTDMPDAD-VAATRKLLLETGFEEpIFELNSHDPQSVQQLVDYLAS 144
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
 26-143 1.05e-08

E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is a multifunctional GTPase found in all bacteria except some eubacteria. It binds to the 16S ribosomal RNA (rRNA) of the 30S subunit and appears to play a role in the assembly of the 30S subunit, possibly by chaperoning the 16S rRNA. It also contacts several assembly elements of the 30S subunit. Era couples cell growth with cytokinesis and plays a role in cell division and energy metabolism. Homologs have also been found in eukaryotes. Era contains two domains: the N-terminal GTPase domain and a C-terminal domain KH domain that is critical for RNA binding. Both domains are important for Era function. Era is functionally able to compensate for deletion of RbfA, a cold-shock adaptation protein that is required for efficient processing of the 16S rRNA.


Pssm-ID: 206726 [Multi-domain]  Cd Length: 168  Bit Score: 51.31  E-value: 1.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446749021  26 LHYKKTQAIewspmAIDTPG----EYLENRCLYSALLTSACEADVIALVLNADaqwSPFSPG------FTAPMNRPTIGL 95
Cdd:cd04163   46 YTDDDAQII-----FVDTPGihkpKKKLGERMVKAAWSALKDVDLVLFVVDAS---EWIGEGdefileLLKKSKTPVILV 117

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 446749021  96 VTKADLA-EPQRISLVAEWLTQAGAQQ-IFITSALNNSGLDAVLDFLNSK 143
Cdd:cd04163  118 LNKIDLVkDKEDLLPLLEKLKELHPFAeIFPISALKGENVDELLEYIVEY 167
 
Name Accession Description Interval E-value
PduV-EutP pfam10662
Ethanolamine utilization - propanediol utilization; Members of this family function in ...
 1-136 1.99e-85

Ethanolamine utilization - propanediol utilization; Members of this family function in ethanolamine and propanediol degradation pathways. PduV may be involved in the association of the bacterial microcompartments (BMCs) to filaments.


Pssm-ID: 402341 [Multi-domain]  Cd Length: 137  Bit Score: 246.04  E-value: 1.99e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446749021    1 MKRLMFIGPSQCGKTSLTQSLRGEALHYKKTQAIEWSPMAIDTPGEYLENRCLYSALLTSACEADVIALVLNADAQWSPF 80
Cdd:pfam10662   1 MKKIMLIGPTGCGKTTLCQALSGEELKYKKTQAIEFYDNAIDTPGEYLENRRYYSALIVTSADADVIALVQDATEPESTF 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 446749021   81 SPGFTAPMNRPTIGLVTKADLAE-PQRISLVAEWLTQAGAQQIFITSALNNSGLDAV 136
Cdd:pfam10662  81 PPGFASMFNKPVIGIITKIDLAKdEANIEIAEEWLSLAGAQKIFRISAVEKIGIEEL 137
EutP TIGR02528
ethanolamine utilization protein, EutP; This protein is found within operons which code for ...
 2-142 7.51e-83

ethanolamine utilization protein, EutP; This protein is found within operons which code for polyhedral organelles containing the enzyme ethanolamine ammonia lyase. The function of this gene is unknown, although the presence of an N-terminal GxxGxGK motif implies a GTP-binding site. [Energy metabolism, Amino acids and amines]


Pssm-ID: 131580 [Multi-domain]  Cd Length: 142  Bit Score: 239.65  E-value: 7.51e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446749021    2 KRLMFIGPSQCGKTSLTQSLRGEALHYKKTQAIEWSPMAIDTPGEYLENRCLYSALLTSACEADVIALVLNADAQWSPFS 81
Cdd:TIGR02528   1 KRIMFIGSVGCGKTTLTQALQGEEILYKKTQAVEYNDGAIDTPGEYVENRRLYSALIVTAADADVIALVQSATDPESRFP 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446749021   82 PGFTAPMNRPTIGLVTKADLAE-PQRISLVAEWLTQAGAQQIFITSALNNSGLDAVLDFLNS 142
Cdd:TIGR02528  81 PGFASIFVKPVIGLVTKIDLAEaDVDIERAKELLETAGAEPIFEISSVDEQGLEALVDYLNS 142
EutP COG4917
Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport ...
 1-144 2.12e-77

Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport and metabolism];


Pssm-ID: 443945 [Multi-domain]  Cd Length: 145  Bit Score: 226.22  E-value: 2.12e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446749021   1 MKRLMFIGPSQCGKTSLTQSLRGEALHYKKTQAIEWSPMAIDTPGEYLENRCLYSALLTSACEADVIALVLNADAQWSPF 80
Cdd:COG4917    1 MKRIMLIGRSGAGKTTLTQALNGEELEYRKTQAVEYYDNIIDTPGEYIENPRFYKALIATAQDADVIVLVQDATEPRSVF 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446749021  81 SPGFTAPMNRPTIGLVTKADLAEPQrISLVAEWLTQAGAQQIFITSALNNSGLDAVLDFLNSKE 144
Cdd:COG4917   81 PPGFAKAFNKPVIGVITKIDLPEAD-VERARKWLKSAGVEPIFIVSSVTGEGIEELKEYLEELG 143
PRK15467 PRK15467
ethanolamine utilization acetate kinase EutP;
1-142 1.32e-13

ethanolamine utilization acetate kinase EutP;


Pssm-ID: 185364 [Multi-domain]  Cd Length: 158  Bit Score: 64.22  E-value: 1.32e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446749021   1 MKRLMFIGPSQCGKTSLTQSLRGEALHYKKTQAIEWSPMA-IDTPGEYLENRCLYSALLTSACEADVIALVLNADAQWSP 79
Cdd:PRK15467   1 MKRIAFVGAVGAGKTTLFNALQGNYTLARKTQAVEFNDKGdIDTPGEYFSHPRWYHALITTLQDVDMLIYVHGANDPESR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446749021  80 FSPG-FTAPMNRPTIGLVTKADLAEPQrISLVAEWLTQAGAQQ-IFITSALNNSGLDAVLDFLNS 142
Cdd:PRK15467  81 LPAGlLDIGVSKRQIAVISKTDMPDAD-VAATRKLLLETGFEEpIFELNSHDPQSVQQLVDYLAS 144
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
41-140 3.89e-11

GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 59.23  E-value: 3.89e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446749021  41 IDTPG----EYLENRCLYSALLTSACEADVIALVLNADAQWSPfspGFT------APMNRPTIGLVTKADLAEPQRI-SL 109
Cdd:COG1159   56 VDTPGihkpKRKLGRRMNKAAWSALEDVDVILFVVDATEKIGE---GDEfilellKKLKTPVILVINKIDLVKKEELlPL 132

                         90       100       110
                 ....*....|....*....|....*....|.
gi 446749021 110 VAEWLTQAGAQQIFITSALNNSGLDAVLDFL 140
Cdd:COG1159  133 LAEYSELLDFAEIVPISALKGDNVDELLDEI 163
era PRK00089
GTPase Era; Reviewed
 26-140 2.61e-09

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 53.90  E-value: 2.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446749021  26 LHYKKTQAIewspmAIDTPG----EYLENRCLYSALLTSACEADVIALVLNADAQWSP---FSPGFTAPMNRPTIGLVTK 98
Cdd:PRK00089  48 VTEDDAQII-----FVDTPGihkpKRALNRAMNKAAWSSLKDVDLVLFVVDADEKIGPgdeFILEKLKKVKTPVILVLNK 122

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 446749021  99 ADLAEPQRI--SLVAEWLTQAGAQQIFITSALNNSGLDAVLDFL 140
Cdd:PRK00089 123 IDLVKDKEEllPLLEELSELMDFAEIVPISALKGDNVDELLDVI 166
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
 26-143 1.05e-08

E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is a multifunctional GTPase found in all bacteria except some eubacteria. It binds to the 16S ribosomal RNA (rRNA) of the 30S subunit and appears to play a role in the assembly of the 30S subunit, possibly by chaperoning the 16S rRNA. It also contacts several assembly elements of the 30S subunit. Era couples cell growth with cytokinesis and plays a role in cell division and energy metabolism. Homologs have also been found in eukaryotes. Era contains two domains: the N-terminal GTPase domain and a C-terminal domain KH domain that is critical for RNA binding. Both domains are important for Era function. Era is functionally able to compensate for deletion of RbfA, a cold-shock adaptation protein that is required for efficient processing of the 16S rRNA.


Pssm-ID: 206726 [Multi-domain]  Cd Length: 168  Bit Score: 51.31  E-value: 1.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446749021  26 LHYKKTQAIewspmAIDTPG----EYLENRCLYSALLTSACEADVIALVLNADaqwSPFSPG------FTAPMNRPTIGL 95
Cdd:cd04163   46 YTDDDAQII-----FVDTPGihkpKKKLGERMVKAAWSALKDVDLVLFVVDAS---EWIGEGdefileLLKKSKTPVILV 117

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 446749021  96 VTKADLA-EPQRISLVAEWLTQAGAQQ-IFITSALNNSGLDAVLDFLNSK 143
Cdd:cd04163  118 LNKIDLVkDKEDLLPLLEKLKELHPFAeIFPISALKGENVDELLEYIVEY 167
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 6-140 7.02e-07

Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.


Pssm-ID: 206648 [Multi-domain]  Cd Length: 161  Bit Score: 46.30  E-value: 7.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446749021   6 FIGPSQCGKTSLTQSLRGEAL-----HYKKTQAIE---WSPMA-------IDTPG----EYLENRCLYSALLTsacEADV 66
Cdd:cd00882    2 VVGRGGVGKSSLLNALLGGEVgevsdVPGTTRDPDvyvKELDKgkvklvlVDTPGldefGGLGREELARLLLR---GADL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446749021  67 IALVLNAD-----AQWSPFSPGFTAPMNRPTIGLVTKADL--AEPQRISLVAEWLTQAGAQQIFITSALNNSGLDAVLDF 139
Cdd:cd00882   79 ILLVVDSTdreseEDAKLLILRRLRKEGIPIILVGNKIDLleEREVEELLRLEELAKILGVPVFEVSAKTGEGVDELFEK 158


                 .
gi 446749021 140 L 140
Cdd:cd00882  159 L 159
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 2-142 3.50e-05

small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 41.59  E-value: 3.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446749021    2 KRLMFIGPSQCGKTSLTQSLRG------EA-----LHYKKTQaIEWSPMA-----IDTPG--EYLENRCLY-SALLTSAC 62
Cdd:TIGR00231   2 IKIVIVGHPNVGKSTLLNSLLGnkgsitEYypgttRNYVTTV-IEEDGKTykfnlLDTAGqeDYDAIRRLYyPQVERSLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446749021   63 EADVIALVLnaDAQWSPFSPGFT----APMNRPTIGLVTKADL----AEPQRISLVAEWltqaGAQQIFITSALNNSGLD 134
Cdd:TIGR00231  81 VFDIVILVL--DVEEILEKQTKEiihhADSGVPIILVGNKIDLkdadLKTHVASEFAKL----NGEPIIPLSAETGKNID 154


                  ....*...
gi 446749021  135 AVLDFLNS 142
Cdd:TIGR00231 155 SAFKIVEA 162
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
 90-143 5.46e-05

Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.


Pssm-ID: 206747 [Multi-domain]  Cd Length: 211  Bit Score: 41.23  E-value: 5.46e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446749021  90 RPTIgLVTKADLAEPQRISLVAEWLTQAGAQqIFITSALNNSGLDAVLDFLNSK 143
Cdd:cd01854   35 EPVI-VLNKADLVDDEELEELLEIYEKLGYP-VLAVSAKTGEGLDELRELLKGK 86
trmE cd04164
trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in ...
 63-138 8.60e-04

trmE is a tRNA modification GTPase; TrmE (MnmE, ThdF, MSS1) is a 3-domain protein found in bacteria and eukaryotes. It controls modification of the uridine at the wobble position (U34) of tRNAs that read codons ending with A or G in the mixed codon family boxes. TrmE contains a GTPase domain that forms a canonical Ras-like fold. It functions a molecular switch GTPase, and apparently uses a conformational change associated with GTP hydrolysis to promote the tRNA modification reaction, in which the conserved cysteine in the C-terminal domain is thought to function as a catalytic residue. In bacteria that are able to survive in extremely low pH conditions, TrmE regulates glutamate-dependent acid resistance.


Pssm-ID: 206727 [Multi-domain]  Cd Length: 159  Bit Score: 37.47  E-value: 8.60e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446749021  63 EADVIALVLNADAQWSPFSPGFTA-PMNRPTIGLVTKADLAEPQRISLVAEwltqaGAQQIFItSALNNSGLDAVLD 138
Cdd:cd04164   82 EADLVLLVVDASEGLDEEDLEILElPAKKPVIVVLNKSDLLSDAEGISELN-----GKPIIAI-SAKTGEGIDELKE 152
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 13-140 1.05e-03

SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec, and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains bacterial SelBs, as well as, one from archaea.


Pssm-ID: 206734 [Multi-domain]  Cd Length: 170  Bit Score: 37.20  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446749021  13 GKTSLTQSLRG-EALHYKKTQA----IE----WSPMA-------IDTPG--EYLENrclysaLLTSACEADVIALVLNAD 74
Cdd:cd04171   11 GKTTLIKALTGiETDRLPEEKKrgitIDlgfaYLDLPdgkrlgfIDVPGheKFVKN------MLAGAGGIDAVLLVVAAD 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446749021  75 AQWSPFSPGFTA---PMNRPTIGLV-TKADLAEPQRISLVAEWLTQ-------AGAqQIFITSALNNSGLDAVLDFL 140
Cdd:cd04171   85 EGIMPQTREHLEileLLGIKKGLVVlTKADLVDEDRLELVEEEILEllagtflADA-PIFPVSSVTGEGIEELKNYL 160
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 94-140 1.70e-03

Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure and biogenesis]; Selenocysteine-specific translation elongation factor SelB is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 442507 [Multi-domain]  Cd Length: 630  Bit Score: 37.59  E-value: 1.70e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446749021  94 GLV--TKADLAEPQRISLV----AEWLTQ---AGAqQIFITSALNNSGLDAVLDFL 140
Cdd:COG3276  107 GIVvlTKADLVDEEWLELVeeeiRELLAGtflEDA-PIVPVSAVTGEGIDELRAAL 161
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
 6-142 1.88e-03

YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli YihA, an essential protein involved in cell division control. YihA and its orthologs are small proteins that typically contain less than 200 amino acid residues and consists of the GTPase domain only (some of the eukaryotic homologs contain an N-terminal extension of about 120 residues that might be involved in organellar targeting). Homologs of yihA are found in most Gram-positive and Gram-negative pathogenic bacteria, with the exception of Mycobacterium tuberculosis. The broad-spectrum nature of YihA and its essentiality for cell viability in bacteria make it an attractive antibacterial target.


Pssm-ID: 206665 [Multi-domain]  Cd Length: 170  Bit Score: 36.72  E-value: 1.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446749021   6 FIGPSQCGKTSLTQSL---RGEALHYK---KTQAI---EWSP--MAIDTPG-------------------EYLENR-CLY 54
Cdd:cd01876    4 FAGRSNVGKSSLINALtnrKKLARTSKtpgRTQLInffNVGDkfRLVDLPGygyakvskevrekwgklieEYLENReNLK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446749021  55 SALLtsaceadviaLVlnaDAQWsPFSP------GFTAPMNRPTIGLVTKADL----AEPQRISLVAEWLTQAGA-QQIF 123
Cdd:cd01876   84 GVVL----------LI---DARH-GPTPidlemlEFLEELGIPFLIVLTKADKlkksELAKVLKKIKEELNLFNIlPPVI 149

                        170
                 ....*....|....*....
gi 446749021 124 ITSALNNSGLDAVLDFLNS 142
Cdd:cd01876  150 LFSSKKGTGIDELRALIAE 168
MnmE COG0486
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ...
 63-140 3.12e-03

tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal structure and biogenesis]; tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440253 [Multi-domain]  Cd Length: 448  Bit Score: 36.58  E-value: 3.12e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446749021  63 EADVIALVLNADAQWSPFSPG-FTAPMNRPTIGLVTKADLAEPQrislvAEWLTQAGAQQIFITSALNNSGLDAVLDFL 140
Cdd:COG0486  292 EADLVLLLLDASEPLTEEDEEiLEKLKDKPVIVVLNKIDLPSEA-----DGELKSLPGEPVIAISAKTGEGIDELKEAI 365
MnmE_helical pfam12631
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ...
 63-142 6.02e-03

MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An N-terminal domain, a helical domain and a GTPase domain which is nested within the helical domain. This family represents the helical domain.


Pssm-ID: 463649 [Multi-domain]  Cd Length: 326  Bit Score: 35.53  E-value: 6.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446749021   63 EADVIALVLNADAQWSPFSPGF--TAPMNRPTIGLVTKADLAEpqrislVAEWLTQAGAQQIFITSALNNSGLDAVLDFL 140
Cdd:pfam12631 173 EADLVLLVLDASRPLDEEDLEIleLLKDKKPIIVVLNKSDLLG------EIDELEELKGKPVLAISAKTGEGLDELEEAI 246


                  ..
gi 446749021  141 NS 142
Cdd:pfam12631 247 KE 248
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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